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Protein

Atrial natriuretic peptide receptor 2

Gene

NPR2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Receptor for the C-type natriuretic peptide NPPC/CNP hormone. Has guanylate cyclase activity upon binding of its ligand. May play a role in the regulation of skeletal growth.2 Publications

Catalytic activityi

GTP = 3',5'-cyclic GMP + diphosphate.

GO - Molecular functioni

  1. ATP binding Source: InterPro
  2. GTP binding Source: UniProtKB-KW
  3. guanylate cyclase activity Source: UniProtKB
  4. hormone binding Source: UniProtKB
  5. natriuretic peptide receptor activity Source: UniProtKB
  6. peptide hormone binding Source: Ensembl
  7. protein kinase activity Source: InterPro
  8. receptor activity Source: ProtInc
  9. transmembrane signaling receptor activity Source: ProtInc

GO - Biological processi

  1. bone development Source: Ensembl
  2. cell surface receptor signaling pathway Source: ProtInc
  3. cellular response to granulocyte macrophage colony-stimulating factor stimulus Source: UniProtKB
  4. cGMP biosynthetic process Source: UniProtKB
  5. intracellular signal transduction Source: InterPro
  6. negative regulation of meiotic cell cycle Source: Ensembl
  7. negative regulation of oocyte maturation Source: Ensembl
  8. ossification Source: UniProtKB-KW
  9. receptor guanylyl cyclase signaling pathway Source: UniProtKB
  10. regulation of blood pressure Source: ProtInc
  11. signal transduction Source: ProtInc
  12. single organism reproductive process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Receptor

Keywords - Biological processi

cGMP biosynthesis, Osteogenesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi4.6.1.2. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Atrial natriuretic peptide receptor 2 (EC:4.6.1.2)
Alternative name(s):
Atrial natriuretic peptide receptor type B
Short name:
ANP-B
Short name:
ANPR-B
Short name:
NPR-B
Guanylate cyclase B
Short name:
GC-B
Gene namesi
Name:NPR2
Synonyms:ANPRB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:7944. NPR2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 458436ExtracellularSequence AnalysisAdd
BLAST
Transmembranei459 – 47820HelicalSequence AnalysisAdd
BLAST
Topological domaini479 – 1047569CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Acromesomelic dysplasia, Maroteaux type (AMDM)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn autosomal recessive acromesomelic chondrodysplasia. Acromesomelic chondrodysplasias are rare hereditary skeletal disorders characterized by short stature, very short limbs and hand/foot malformations. The severity of limb abnormalities increases from proximal to distal with profoundly affected hands and feet showing brachydactyly and/or rudimentary fingers (knob-like fingers). AMDM is characterized by axial skeletal involvement with wedging of vertebral bodies. In AMDM all skeletal elements are present but show abnormal rates of linear growth.

See also OMIM:602875
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti32 – 321P → T in AMDM. 1 Publication
Corresponds to variant rs28931581 [ dbSNP | Ensembl ].
VAR_022583
Natural varianti115 – 1151W → G in AMDM; markedly deficient activity. 1 Publication
Corresponds to variant rs28931582 [ dbSNP | Ensembl ].
VAR_022584
Natural varianti176 – 1761D → E in AMDM. 1 Publication
Corresponds to variant rs28929479 [ dbSNP | Ensembl ].
VAR_022585
Natural varianti297 – 2971T → M in AMDM; markedly deficient activity. 1 Publication
VAR_022586
Natural varianti338 – 3381Y → C in AMDM. 1 Publication
VAR_022587
Natural varianti409 – 4091A → T in AMDM. 1 Publication
VAR_022588
Natural varianti413 – 4131G → E in AMDM; markedly deficient activity. 1 Publication
VAR_022589
Natural varianti708 – 7081Y → C in AMDM. 1 Publication
VAR_022590
Natural varianti776 – 7761R → W in AMDM. 1 Publication
VAR_022591
Natural varianti957 – 9571R → C in AMDM. 1 Publication
VAR_022592
Natural varianti959 – 9591G → A in AMDM. 1 Publication
VAR_022593
Epiphyseal chondrodysplasia, Miura type (ECDM)4 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn overgrowth syndrome characterized by tall stature, long hands and feet with arachnodactyly, macrodactyly of the great toes, scoliosis, coxa valga and slipped capital femoral epiphysis.

See also OMIM:615923
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti488 – 4881A → P in ECDM; mutant and wild-type alleles have similar expression levels; the mutation results in increased guanylate cyclase activity. 1 Publication
VAR_071875
Natural varianti655 – 6551R → C in ECDM; the mutation results in increased guanylate cyclase activity. 1 Publication
VAR_071876
Natural varianti882 – 8821V → M in ECDM; the mutation results in higher guanylate cyclase activity; causes a 15-fold increase in basal Vmax; has higher affinity for GTP than wild-type in the presence of NPPC; might lead to a structural change that locks the enzyme in a conformation mimicking the ATP-bound state. 2 Publications
VAR_071877

Keywords - Diseasei

Disease mutation, Dwarfism

Organism-specific databases

MIMi602875. phenotype.
615923. phenotype.
Orphaneti40. Acromesomelic dysplasia, Maroteaux type.
329191. Tall stature - scoliosis - macrodactyly of the great toes.
PharmGKBiPA257.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 10471025Atrial natriuretic peptide receptor 2PRO_0000012364Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi24 – 241N-linked (GlcNAc...)Sequence Analysis
Glycosylationi35 – 351N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi75 ↔ 101By similarity
Glycosylationi161 – 1611N-linked (GlcNAc...)Sequence Analysis
Glycosylationi195 – 1951N-linked (GlcNAc...)Sequence Analysis
Glycosylationi244 – 2441N-linked (GlcNAc...)Sequence Analysis
Glycosylationi277 – 2771N-linked (GlcNAc...)Sequence Analysis
Glycosylationi349 – 3491N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi439 – 439InterchainCurated
Disulfide bondi448 – 448InterchainCurated
Modified residuei513 – 5131Phosphoserine1 Publication
Modified residuei516 – 5161Phosphothreonine1 Publication
Modified residuei518 – 5181Phosphoserine1 Publication
Modified residuei522 – 5221PhosphoserineBy similarity
Modified residuei523 – 5231Phosphoserine1 Publication
Modified residuei526 – 5261Phosphoserine1 Publication
Modified residuei529 – 5291Phosphothreonine1 Publication

Post-translational modificationi

Phosphorylation of the protein kinase-like domain is required for full activation by CNP.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP20594.
PaxDbiP20594.
PRIDEiP20594.

PTM databases

PhosphoSiteiP20594.

Expressioni

Gene expression databases

BgeeiP20594.
CleanExiHS_NPR2.
ExpressionAtlasiP20594. baseline and differential.
GenevestigatoriP20594.

Organism-specific databases

HPAiHPA011977.

Interactioni

Protein-protein interaction databases

BioGridi110942. 5 interactions.
IntActiP20594. 2 interactions.
STRINGi9606.ENSP00000341083.

Structurei

3D structure databases

ProteinModelPortaliP20594.
SMRiP20594. Positions 24-442, 503-832, 852-1025.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini513 – 786274Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini861 – 991131Guanylate cyclasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.PROSITE-ProRule annotation
Contains 1 guanylate cyclase domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118959.
HOVERGENiHBG051862.
InParanoidiP20594.
KOiK12324.
OMAiAAKSEHY.
OrthoDBiEOG7Z69BJ.
PhylomeDBiP20594.
TreeFamiTF106338.

Family and domain databases

Gene3Di3.30.70.1230. 1 hit.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR001828. ANF_lig-bd_rcpt.
IPR011009. Kinase-like_dom.
IPR001170. Ntpep_rcpt.
IPR029787. Nucleotide_cyclase.
IPR028082. Peripla_BP_I.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF01094. ANF_receptor. 1 hit.
PF00211. Guanylate_cyc. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR00255. NATPEPTIDER.
SMARTiSM00044. CYCc. 1 hit.
[Graphical view]
SUPFAMiSSF53822. SSF53822. 1 hit.
SSF55073. SSF55073. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00458. ANF_RECEPTORS. 1 hit.
PS00452. GUANYLATE_CYCLASE_1. 1 hit.
PS50125. GUANYLATE_CYCLASE_2. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Long (identifier: P20594-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MALPSLLLLV AALAGGVRPP GARNLTLAVV LPEHNLSYAW AWPRVGPAVA
60 70 80 90 100
LAVEALGRAL PVDLRFVSSE LEGACSEYLA PLSAVDLKLY HDPDLLLGPG
110 120 130 140 150
CVYPAASVAR FASHWRLPLL TAGAVASGFS AKNDHYRTLV RTGPSAPKLG
160 170 180 190 200
EFVVTLHGHF NWTARAALLY LDARTDDRPH YFTIEGVFEA LQGSNLSVQH
210 220 230 240 250
QVYAREPGGP EQATHFIRAN GRIVYICGPL EMLHEILLQA QRENLTNGDY
260 270 280 290 300
VFFYLDVFGE SLRAGPTRAT GRPWQDNRTR EQAQALREAF QTVLVITYRE
310 320 330 340 350
PPNPEYQEFQ NRLLIRARED FGVELGPSLM NLIAGCFYDG ILLYAEVLNE
360 370 380 390 400
TIQEGGTRED GLRIVEKMQG RRYHGVTGLV VMDKNNDRET DFVLWAMGDL
410 420 430 440 450
DSGDFQPAAH YSGAEKQIWW TGRPIPWVKG APPSDNPPCA FDLDDPSCDK
460 470 480 490 500
TPLSTLAIVA LGTGITFIMF GVSSFLIFRK LMLEKELASM LWRIRWEELQ
510 520 530 540 550
FGNSERYHKG AGSRLTLSLR GSSYGSLMTA HGKYQIFANT GHFKGNVVAI
560 570 580 590 600
KHVNKKRIEL TRQVLFELKH MRDVQFNHLT RFIGACIDPP NICIVTEYCP
610 620 630 640 650
RGSLQDILEN DSINLDWMFR YSLINDLVKG MAFLHNSIIS SHGSLKSSNC
660 670 680 690 700
VVDSRFVLKI TDYGLASFRS TAEPDDSHAL YAKKLWTAPE LLSGNPLPTT
710 720 730 740 750
GMQKADVYSF GIILQEIALR SGPFYLEGLD LSPKEIVQKV RNGQRPYFRP
760 770 780 790 800
SIDRTQLNEE LVLLMERCWA QDPAERPDFG QIKGFIRRFN KEGGTSILDN
810 820 830 840 850
LLLRMEQYAN NLEKLVEERT QAYLEEKRKA EALLYQILPH SVAEQLKRGE
860 870 880 890 900
TVQAEAFDSV TIYFSDIVGF TALSAESTPM QVVTLLNDLY TCFDAIIDNF
910 920 930 940 950
DVYKVETIGD AYMVVSGLPG RNGQRHAPEI ARMALALLDA VSSFRIRHRP
960 970 980 990 1000
HDQLRLRIGV HTGPVCAGVV GLKMPRYCLF GDTVNTASRM ESNGQALKIH
1010 1020 1030 1040
VSSTTKDALD ELGCFQLELR GDVEMKGKGK MRTYWLLGER KGPPGLL
Length:1,047
Mass (Da):117,022
Last modified:February 1, 1991 - v1
Checksum:i817FB74D6B31F7EF
GO
Isoform Short (identifier: P20594-2) [UniParc]FASTAAdd to basket

Also known as: NPR-BI

The sequence of this isoform differs from the canonical sequence as follows:
     964-1047: PVCAGVVGLK...GERKGPPGLL → KADSHSSPSLHLSQTLPTCFFSKGQSVLGLLA

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Show »
Length:995
Mass (Da):111,208
Checksum:i745D41E451E0D7DF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti755 – 7551T → S in BAA81737 (PubMed:10082481).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti32 – 321P → T in AMDM. 1 Publication
Corresponds to variant rs28931581 [ dbSNP | Ensembl ].
VAR_022583
Natural varianti115 – 1151W → G in AMDM; markedly deficient activity. 1 Publication
Corresponds to variant rs28931582 [ dbSNP | Ensembl ].
VAR_022584
Natural varianti176 – 1761D → E in AMDM. 1 Publication
Corresponds to variant rs28929479 [ dbSNP | Ensembl ].
VAR_022585
Natural varianti232 – 2321M → I.1 Publication
Corresponds to variant rs55747238 [ dbSNP | Ensembl ].
VAR_042219
Natural varianti297 – 2971T → M in AMDM; markedly deficient activity. 1 Publication
VAR_022586
Natural varianti338 – 3381Y → C in AMDM. 1 Publication
VAR_022587
Natural varianti409 – 4091A → T in AMDM. 1 Publication
VAR_022588
Natural varianti413 – 4131G → E in AMDM; markedly deficient activity. 1 Publication
VAR_022589
Natural varianti488 – 4881A → P in ECDM; mutant and wild-type alleles have similar expression levels; the mutation results in increased guanylate cyclase activity. 1 Publication
VAR_071875
Natural varianti655 – 6551R → C in ECDM; the mutation results in increased guanylate cyclase activity. 1 Publication
VAR_071876
Natural varianti708 – 7081Y → C in AMDM. 1 Publication
VAR_022590
Natural varianti771 – 7711Q → E.
Corresponds to variant rs5816 [ dbSNP | Ensembl ].
VAR_011968
Natural varianti776 – 7761R → W in AMDM. 1 Publication
VAR_022591
Natural varianti882 – 8821V → I.1 Publication
Corresponds to variant rs55700371 [ dbSNP | Ensembl ].
VAR_042220
Natural varianti882 – 8821V → M in ECDM; the mutation results in higher guanylate cyclase activity; causes a 15-fold increase in basal Vmax; has higher affinity for GTP than wild-type in the presence of NPPC; might lead to a structural change that locks the enzyme in a conformation mimicking the ATP-bound state. 2 Publications
VAR_071877
Natural varianti957 – 9571R → C in AMDM. 1 Publication
VAR_022592
Natural varianti959 – 9591G → A in AMDM. 1 Publication
VAR_022593

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei964 – 104784PVCAG…PPGLL → KADSHSSPSLHLSQTLPTCF FSKGQSVLGLLA in isoform Short. 1 PublicationVSP_001810Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB005647 Genomic DNA. Translation: BAA81737.1.
AJ005282 mRNA. Translation: CAA06466.1.
AL133410 Genomic DNA. Translation: CAI10987.1.
EU326311 Genomic DNA. Translation: ACA05920.1.
EU326311 Genomic DNA. Translation: ACA05921.1.
CH471071 Genomic DNA. Translation: EAW58338.1.
CH471071 Genomic DNA. Translation: EAW58337.1.
CH471071 Genomic DNA. Translation: EAW58339.1.
CH471071 Genomic DNA. Translation: EAW58340.1.
BC023017 mRNA. Translation: AAH23017.1.
CCDSiCCDS6590.1. [P20594-1]
PIRiS05514. OYHUBR.
RefSeqiNP_003986.2. NM_003995.3. [P20594-1]
UniGeneiHs.78518.

Genome annotation databases

EnsembliENST00000342694; ENSP00000341083; ENSG00000159899. [P20594-1]
GeneIDi4882.
KEGGihsa:4882.
UCSCiuc003zyd.3. human. [P20594-1]

Polymorphism databases

DMDMi113916.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB005647 Genomic DNA. Translation: BAA81737.1.
AJ005282 mRNA. Translation: CAA06466.1.
AL133410 Genomic DNA. Translation: CAI10987.1.
EU326311 Genomic DNA. Translation: ACA05920.1.
EU326311 Genomic DNA. Translation: ACA05921.1.
CH471071 Genomic DNA. Translation: EAW58338.1.
CH471071 Genomic DNA. Translation: EAW58337.1.
CH471071 Genomic DNA. Translation: EAW58339.1.
CH471071 Genomic DNA. Translation: EAW58340.1.
BC023017 mRNA. Translation: AAH23017.1.
CCDSiCCDS6590.1. [P20594-1]
PIRiS05514. OYHUBR.
RefSeqiNP_003986.2. NM_003995.3. [P20594-1]
UniGeneiHs.78518.

3D structure databases

ProteinModelPortaliP20594.
SMRiP20594. Positions 24-442, 503-832, 852-1025.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110942. 5 interactions.
IntActiP20594. 2 interactions.
STRINGi9606.ENSP00000341083.

Chemistry

ChEMBLiCHEMBL2111337.
DrugBankiDB01613. Erythrityl Tetranitrate.
DB04899. Nesiritide.
GuidetoPHARMACOLOGYi1748.

PTM databases

PhosphoSiteiP20594.

Polymorphism databases

DMDMi113916.

Proteomic databases

MaxQBiP20594.
PaxDbiP20594.
PRIDEiP20594.

Protocols and materials databases

DNASUi4882.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000342694; ENSP00000341083; ENSG00000159899. [P20594-1]
GeneIDi4882.
KEGGihsa:4882.
UCSCiuc003zyd.3. human. [P20594-1]

Organism-specific databases

CTDi4882.
GeneCardsiGC09P035792.
H-InvDBHIX0034787.
HGNCiHGNC:7944. NPR2.
HPAiHPA011977.
MIMi108961. gene.
602875. phenotype.
615923. phenotype.
neXtProtiNX_P20594.
Orphaneti40. Acromesomelic dysplasia, Maroteaux type.
329191. Tall stature - scoliosis - macrodactyly of the great toes.
PharmGKBiPA257.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118959.
HOVERGENiHBG051862.
InParanoidiP20594.
KOiK12324.
OMAiAAKSEHY.
OrthoDBiEOG7Z69BJ.
PhylomeDBiP20594.
TreeFamiTF106338.

Enzyme and pathway databases

BRENDAi4.6.1.2. 2681.

Miscellaneous databases

ChiTaRSiNPR2. human.
GeneWikiiNPR2.
GenomeRNAii4882.
NextBioi18792.
PROiP20594.
SOURCEiSearch...

Gene expression databases

BgeeiP20594.
CleanExiHS_NPR2.
ExpressionAtlasiP20594. baseline and differential.
GenevestigatoriP20594.

Family and domain databases

Gene3Di3.30.70.1230. 1 hit.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR001828. ANF_lig-bd_rcpt.
IPR011009. Kinase-like_dom.
IPR001170. Ntpep_rcpt.
IPR029787. Nucleotide_cyclase.
IPR028082. Peripla_BP_I.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF01094. ANF_receptor. 1 hit.
PF00211. Guanylate_cyc. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR00255. NATPEPTIDER.
SMARTiSM00044. CYCc. 1 hit.
[Graphical view]
SUPFAMiSSF53822. SSF53822. 1 hit.
SSF55073. SSF55073. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00458. ANF_RECEPTORS. 1 hit.
PS00452. GUANYLATE_CYCLASE_1. 1 hit.
PS50125. GUANYLATE_CYCLASE_2. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Differential activation by atrial and brain natriuretic peptides of two different receptor guanylate cyclases."
    Chang M.S., Lowe D.G., Lewis M., Hellmiss R., Chen E., Goeddel D.V.
    Nature 341:68-72(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE (ISOFORM LONG).
    Tissue: Brain.
  2. "Structure of the type B human natriuretic peptide receptor gene and association of a novel microsatellite polymorphism with essential hypertension."
    Rehemudula D., Nakayama T., Soma M., Takahashi Y., Uwabo J., Sato M., Izumi Y., Kanmatsuse K., Ozawa Y.
    Circ. Res. 84:605-610(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Blood.
  3. "cGMP-dependent and -independent inhibition of a K+ conductance by natriuretic peptides: molecular and functional studies in human proximal tubule cells."
    Hirsch J.R., Meyer M., Maegert H.-J., Forssmann W.-G., Mollerup S., Herter P., Weber G., Cermak R., Ankorina-Stark I., Schlatter E., Kruhoffer M.
    J. Am. Soc. Nephrol. 10:472-480(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
    Tissue: Kidney.
  4. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. NHLBI resequencing and genotyping service (RS&G)
    Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
    Tissue: Brain.
  8. "Extracellular domain-IgG fusion proteins for three human natriuretic peptide receptors. Hormone pharmacology and application to solid phase screening of synthetic peptide antisera."
    Bennett B.D., Bennett G.L., Vitangcol R.V., Jewett J.R., Burnier J., Henzel W., Lowe D.G.
    J. Biol. Chem. 266:23060-23067(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: LIGAND-BINDING.
  9. "Selective activation of the B natriuretic peptide receptor by C-type natriuretic peptide (CNP)."
    Koller K.J., Lowe D.G., Bennett G.L., Minamino N., Kangawa K., Matsuo H., Goeddel D.V.
    Science 252:120-123(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
  11. Cited for: FUNCTION, VARIANTS AMDM THR-32; GLY-115; GLU-176; MET-297; CYS-338; THR-409; GLU-413; CYS-708; TRP-776; CYS-957 AND ALA-959, CHARACTERIZATION OF VARIANTS AMDM GLY-115; MET-297 AND GLU-413.
  12. "Mass spectrometric identification of phosphorylation sites in guanylyl cyclase A and B."
    Yoder A.R., Stone M.D., Griffin T.J., Potter L.R.
    Biochemistry 49:10137-10145(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-513; THR-516; SER-518; SER-523; SER-526 AND THR-529.
  13. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] ILE-232 AND ILE-882.
  14. "An overgrowth disorder associated with excessive production of cGMP due to a gain-of-function mutation of the natriuretic peptide receptor 2 gene."
    Miura K., Namba N., Fujiwara M., Ohata Y., Ishida H., Kitaoka T., Kubota T., Hirai H., Higuchi C., Tsumaki N., Yoshikawa H., Sakai N., Michigami T., Ozono K.
    PLoS ONE 7:E42180-E42180(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN ECDM, VARIANT ECDM MET-882, CHARACTERIZATION OF VARIANT ECDM MET-882.
  15. "A human skeletal overgrowth mutation increases maximal velocity and blocks desensitization of guanylyl cyclase-B."
    Robinson J.W., Dickey D.M., Miura K., Michigami T., Ozono K., Potter L.R.
    Bone 56:375-382(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT ECDM MET-882.
  16. Cited for: VARIANT ECDM CYS-655, CHARACTERIZATION OF VARIANT ECDM CYS-655.
  17. "Overgrowth syndrome associated with a gain-of-function mutation of the natriuretic peptide receptor 2 (NPR2) gene."
    Miura K., Kim O.H., Lee H.R., Namba N., Michigami T., Yoo W.J., Choi I.H., Ozono K., Cho T.J.
    Am. J. Med. Genet. A 164A:156-163(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ECDM PRO-488, CHARACTERIZATION OF VARIANT ECDM PRO-488.

Entry informationi

Entry nameiANPRB_HUMAN
AccessioniPrimary (citable) accession number: P20594
Secondary accession number(s): B0ZBF2
, B0ZBF3, D3DRP3, D3DRP4, O60871, Q4VAK7, Q5TCV2, Q8TA93, Q9UQ50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: April 1, 2015
This is version 173 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.